ID A0A397GXW8_9GLOM Unreviewed; 1453 AA.
AC A0A397GXW8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Glove_428g91 {ECO:0000313|EMBL:RHZ54344.1};
OS Diversispora epigaea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ54344.1, ECO:0000313|Proteomes:UP000266861};
RN [1] {ECO:0000313|EMBL:RHZ54344.1, ECO:0000313|Proteomes:UP000266861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT104 {ECO:0000313|EMBL:RHZ54344.1,
RC ECO:0000313|Proteomes:UP000266861};
RA Sun X., Fei Z., Harrison M.;
RT "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ54344.1}.
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DR EMBL; PQFF01000379; RHZ54344.1; -; Genomic_DNA.
DR STRING; 1348612.A0A397GXW8; -.
DR Proteomes; UP000266861; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF197; DEPENDENT RNA HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G07950)-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000266861}.
FT DOMAIN 637..810
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 921..1093
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1453 AA; 165835 MW; 67C7987A49F6BE82 CRC64;
MGKKKKATNS VRGFATTSTP SKAKDVTPNE LLDKENPKKA KIDSENTSTK IVTDSTIISE
DIESQRYIEK LRDLNSIKVE AYFEETEKTK NRVDKLPVLK LDVNIEQAVI KHIKKIGYQE
QVNDKIDGKA DREQVLVKLD IIYLILKRLG FLKRDVETCI RKICSLELQS ALDWLCINVS
SESLPIGFAD KLYHEDETDI TFVRTSSSSW QPPVGKTEPP TQNLSIQKTN IPNRDVPRST
KSTKSAILDE KLKSLTLNAL ENINSDSEEE NDPNMKYAVL KYELMGKSTI LKKLEKSKKD
NKTKCDLILN QINQLNSQIK LIEQNYLFSK KTADNIYKKK IKKNDFKEFD LDSDDEEEEE
IEKKEDKDDI DDHENFLGFS IKDEEDGDLF GGLLDIPIST SDDNNNVNSM EVETTDTTNS
TSCALRDMPV PPSWTGQLPK DMLQEFCRKI DSKALVTFSK EPTIGGNSIM KAKVIISWSN
GKLNTFIMKG EGCRTFEEAK DYVSTLALFE LTNLPLYMAL PPSYSDLWKE LIQTKNIAAN
KNTIATEEER MKFLLSIVDN KVKEVMKIQE VTKGDTVSQE SNMMPTKFVP ISKDIKISDE
GKAIKKAFEN RQLNKPYKDL LNVRKKLPMY SYREELLKEL NKNQVVIVSG ETGCGKSTQV
PQFIAEHMIM NELGDHCNIL CTQPRRISAI SIAHRVSLEM GDAPGTTGST KSLVGYQIRL
ESRISRSNVM TFCTNGILLR RLEGDGLLNG VSHVIVDEVH ERTLEIDFLL IILKNLLQKR
HDLKVILMSA TIEAKKLSSH FSGCPLVEVP GRTFPVAIKY LEDVVEETEY MINEGDEYAR
KIYRKIKDEG TITIGRGDSS QKLNYELEED RDMNDDFEFP DEELLSSYSQ RTRLVLRSID
HDKINYDLIL SLLRYICISK DNKSLNTEVP PDGAILIFLP GMPEIIKLYD LLTCDRHFED
ETRFLVFPLH SLISSENQGR VFEIPPEGVR KIVLATNIAE TGITISDVTI VIDTGKVNLV
RYNKQKRITT LEETFVAKAN ARQRRGRAGR IREGICFHLF TKWKHDYNML DYEPPEILRL
PLQELCLKIK ICGMGDISDV LGMAIDPPTP QAIEDAISSL QEVQALTPEQ QLTPLGIHLS
HIPVDVHIGK MLLFGSIFRC LDPILTIAAI LSYKSPFITP FGRESEFNAA RKKFENHNSD
LLTMYKAYCE WKSNYGKSSP IMGEFCQKNF LSDQNLRMID DLKKQYLSLL VNIGFVHIND
RMKVELSRSS YKRSLCIVPE SYNVNSTFTP IINAAIVAGL YPKVIHRDIQ MNQFINRDQK
AVYIHPSSIN YPLQNAKKPN KDWFVYNTMI QTKKLYVRDT SLVEVVDLVL FGRETEVKHE
IKLLTIDKWI KLQCFAKTAT LLKYLREQLN KILKYKIDHP EAELEQEQEE WLNLILGVIK
SCEIDSSPGR VSV
//
